Recent reports have documented the importance of responses to the Group I (e.g., Der p I and Der f I) and Group II (e.g., Der p II and Der f II) protein allergens in house dust mite allergy. For example, it has been documented that over 60% of patients have at least 50% of their anti-mite antibodies directed towards these proteins (e.g., Lind, P. et al., Allergy, 39:259-274 (1984); van der Zee, J. S. et al., Journal Allergy and Clinical Immunology, 81:884-896 (1988)). It is possible that children show a greater degree of reactivity to the Group I and Group II allergens (Thompson, P. J., et al., Immunology, 64:301-314 (1988)). Allergy to mites of the genus Dermatophagoides (D.) is associated with conditions such as asthma, rhinitis and ectopic dermatitis. Two species, D. pteronyssinus and D. farinae, predominate and, as a result, considerable effort has been expended in trying to identify the allergens produced by these two species.
A concerted effort has been made to characterize by gene cloning the major allergens from both D. pteronyssinus and D. farinae. Consequently, several publications have reported the complete nucleotide sequences of several allergens including Der p I (Thomas, W. R., et al., International Archives of Allergy and Applied Immunology. 85:127-129 (1988); and Chua, K. Y., et al., Journal of Experimental Medicine, 167:175-182 (1988)), Der p II (Chua, K. Y., et al., International Archives of Allergy and Applied Immunology, 91:118-123 (1990)), Der f I (Dilworth, R. J., et al., Clinical and Experimental Allergy, 21:25-32 (1891)), Der f II (Yuuki, T., et al., Japan Journal Allergol., 39:557-461 (1990); and Trudinger, M., et al., Clinical and Experimental Allergy, 21:33-37 (1991)) and a low molecular weight allergen (Ovey, E. R., et al., Journal of Experimental Medicine, 170:1457-1462 (1989)).
The published nucleotide sequences of cDNAs encoding Der p I and Der f I demonstrate that these two proteins are highly homologous at the amino acid level (81% identity) and that the mature protein products are comprised of 222 and 223 residues, respectively (Chua, K. Y., et al., Journal of Experimental Medicine, 167:175-182 (1988); and Dilworth, R. J., et al., supra)). The protein allergens Der p II and Der f II are both comprised of 129 residues, and are also highly homologous (88% identity) in amino acid sequence (Trudinger, M., et al. supra; Yuuki, T., et al. supra); Chua, K. Y., et al., International Archives of Allergy and Applied Immunology, 91:118-123 (1990)).
The isolation of cDNAs clones encoding Der p I and Der p II has permitted antibody binding studies on the recombinant antigens (Green, W. K., et al., International Archives of Allergy and Applied Immunology, 92:30-38 (1990); Chua, K. Y., et al., International Archives of Allergy and Applied Immunology, 91:124-129 (1990)). Complementary DNA fragments of Der p I have been expressed in E. coli and IgE binding studies with pooled human mite allergic IgE sera have demonstrated binding and non-binding regions throughout the molecule (Thomas, W. R., et al., In: Epitopes of Atopic Allergens. Proceedings of Workshop from XIV Congress of the European Academy of Allergy and Clinical Immunology, Berlin, September 1989. pp 77-82). T cell epitopes of Der p I have been reported (O'Hehir, R. E., et al., Annual Review Immunology, 9:67-95 (1991); Stewart, G. A., et al., In: Epitopes of Atopic Allergens. Proceedings of Workshop from XIV Congress of the European Academy of Allergy and Clinical Immunology, Berlin, September 1989. pp 41-47; Yessel, H., et al., In: T cell Activation in Health and Disease: Discrimination Between Immunity and Tolerance, Conference 22-26 September, 1990, Trinity College, Oxford, U.K. and Hessel, H., et al., Journal of Immunology, 148(3): 738-745 (Feb. 1, 1992).